ID K0N2C7_DESTT Unreviewed; 435 AA.
AC K0N2C7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=GabT: 4-aminobutyrate aminotransferase (Gamma-amino-N-butyrate transaminase) {ECO:0000313|EMBL:CCK78299.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:CCK78299.1};
GN Name=gabT {ECO:0000313|EMBL:CCK78299.1};
GN OrderedLocusNames=TOL2_C01290 {ECO:0000313|EMBL:CCK78299.1};
OS Desulfobacula toluolica (strain DSM 7467 / Tol2).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulfobacula.
OX NCBI_TaxID=651182 {ECO:0000313|EMBL:CCK78299.1, ECO:0000313|Proteomes:UP000007347};
RN [1] {ECO:0000313|EMBL:CCK78299.1, ECO:0000313|Proteomes:UP000007347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7467 / Tol2 {ECO:0000313|Proteomes:UP000007347};
RX PubMed=23088741; DOI=10.1111/j.1462-2920.2012.02885.x;
RA Wohlbrand L., Jacob J.H., Kube M., Mussmann M., Jarling R., Beck A.,
RA Amann R., Wilkes H., Reinhardt R., Rabus R.;
RT "Complete genome, catabolic sub-proteomes and key-metabolites of
RT Desulfobacula toluolica Tol2, a marine, aromatic compound-degrading,
RT sulfate-reducing bacterium.";
RL Environ. Microbiol. 15:1334-55(2013).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; FO203503; CCK78299.1; -; Genomic_DNA.
DR RefSeq; WP_014955657.1; NC_018645.1.
DR AlphaFoldDB; K0N2C7; -.
DR STRING; 651182.TOL2_C01290; -.
DR KEGG; dto:TOL2_C01290; -.
DR PATRIC; fig|651182.5.peg.160; -.
DR HOGENOM; CLU_016922_10_0_7; -.
DR OrthoDB; 9801834at2; -.
DR Proteomes; UP000007347; Chromosome.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00700; GABAtrnsam; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000313|EMBL:CCK78299.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000007347};
KW Transferase {ECO:0000313|EMBL:CCK78299.1}.
SQ SEQUENCE 435 AA; 47735 MW; 9FA548881692AFDB CRC64;
MTSTKSEYFR KMRQEHVAQG PAHITQAVIQ KASGAVMTDV DGKEFIDFAG GIGVNNVGHS
HPKVVKAIKD QADQFIHTCF HVGMYDSYIE LAARLNDLAP GDFAKKTMFG NSGAEAVENA
VKVARYATKR PAVIAFENGF HGRTLLTMSL TSKIMPYKYG FGPFAPEIYR IPYPYCYRCP
LGCKYPDCNI ACAEYLESYF ITYVDPDSVA AIIAEPIQGE GGFVTPPPEY FPKLAEICKK
HGILLIIDEV QSGAGRTGKF LAIEHWGIEP DIITQAKSLA GGMPLSAITG RQELMDAPHP
GGLGGTYSGN PLSCKAALAV LDILFEDKLL ERSKELGEIL FQRFSELQNS FEIIGDVRGK
GPMLALELVK DRQTREPAAA EAKKLTQLCY EKGLVLLSCG NFGNVIRTLM PFVITDEQLD
KGLSIMEESL RELTK
//
